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植物多酚氧化酶的研究进展 总被引:1,自引:0,他引:1
多酚氧化酶(polyphenol oxidase, PPO)是一类普遍存在于植物、真菌和昆虫质体中,由核基因编码, 能与铜相结合的金属蛋白酶。它能分别催化单酚羟基和二羟基酚氧化为O-二酚和O-醌。植物多酚氧化酶是许多果蔬等农产品酶促褐变的主要原因, 同时它在植物的光合作用、抗病虫害、生长发育以及花色的形成中起一定作用。本文综述了植物多酚氧化酶在细胞学、分子遗传学及其生产应用等方面的研究进展。 相似文献
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富士苹果多酚氧化酶特性研究 总被引:19,自引:0,他引:19
本文从富士苹果中提取和部分纯化多酚氧化酶,并对其特性进行研究。以邻苯二酚为作用底物,该酶最适pH为50,在pH50~80范围内有较高的稳定性。最适温度为30℃,在60℃以上迅速失活。该酶对不同的酚类物质表现出不同的底物专一性,由高至低的趋势依次为邻苯二酚、焦性没食子酸、DL-多巴、酪氨酸,其中对酪氨酸的活力为零。浓度为04mmol/L的VC、L-半胱氨酸及浓度为03mmol/L的亚硫酸氢钠,可完全抑制该酶活性。 相似文献
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莲藕多酚氧化酶同工酶的比较分析 总被引:4,自引:0,他引:4
采用垂直板聚丙烯酰胺凝胶电泳技术,对同一植株莲藕的不同部位、不同湖区野生莲藕以及不同品种的特定部位的多酚氧化酶(PPO)同工酶进行了分析。结果表明,同一植株莲藕不同部位PPO同工酶带有一定的特异性, 其主要表现在区带数目、迁移位置和区带染色深浅三方面;而不同湖区野生莲藕以及不同品种莲藕,处于同一生长周期、同一部位中的PPO同工酶遗传多样性则较低。 相似文献
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为探讨梨果多酚氧化酶(polyphenol oxidase,PPO)活性变化规律,本研究选取贡梨、酸梨、紫酥梨、香梨、酥梨和皇冠梨6个不同品种的砀山梨果作为实验材料,采用分光光度计法分别测定了梨果的皮、肉和心的多酚氧化酶活性,并对其进行分析。结果表明,紫酥梨皮、香梨肉和香梨心PPO活性最高,分别为19.72AU·g-1·min-1、19.51AU·g-1·min-1和19.30AU·g-1·min-1,酸梨皮、酸梨肉以及皇冠梨心的PPO活性最低,分别只有11.64AU·g-1·min-1、13.39AU·g-1·min-1和6.67AU·g-1·min-1。PPO活性变异及方差分析显示,梨皮PPO活性平均值最高为16.27AU·g-1·min-1,梨心PPO活性平均值最低为13.68AU·g-1·min-1;不同品种梨皮、梨肉、梨心PPO活性变化不一致;不同部位中梨心的PPO活性变异系数最大,达32.23%;不同部位及品种间PPO活性差异不显著。由此可知梨皮可以作为梨果PPO活性改良的目标之一,梨心具有筛选低PPO活性的潜力,皇冠梨梨心可作为选育低PPO活性的种质资源。 相似文献
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烟草中多酚氧化酶(PPO)的特征 总被引:3,自引:0,他引:3
烟草中的多酚氧化酶介导的褐变会影响烟叶和烟丝的色泽和内在质量,因此对其特性的研究,以及活性的控制成为多年来的研究热点。本文从其生物发生模型、分子结构、生物化学和光谱学特征与植物抗病和机械损伤的关系,多酚氧化酶的抑制、多酚氧化酶的应用等方面着手,对近几年来烟草中PPO研究的最新成果进行总结和回顾,对一些有争议的问题进行了探讨,并对未来PPO研究的方向和领域进行了展望。 相似文献
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运用丙酮浸漬干燥、磷酸盐缓冲液提取、低温离心、硫酸铵沉淀、DEAE-Sephadex(A-50)、Sephadex(G-75) 和DEAE-celluse(DE-52)层析等方法从苹果中分离获得一种新的含铜酶蛋白,该酶被命名为多酚氧化酶Ⅱ(polyphenol oxidase Ⅱ, PPOⅡ),纯化倍数是215,纯化收率是23%.PAGE、SDS-PAGE和MALDI-TOF 等技术用于测定所获的酶的纯度和分子量.在PAGE和SDS-PAGE 均显示一条带,表明PPOⅡ只由一个亚基组成,且已达到单一组分(MALDI-TOF的结果更证实了这一点).SDS-PAGE 和 MALDI-TOF 的结果都表明PPO的分子量为 38204 Da.pH值对酶活性和稳定性研究的结果显示,从pH值4.0~7.0随着pH值的增加,酶活性也不断增加;从pH值 7.0~11.0, 酶活性不断降低.PPOⅡ的最适pH值为6.6最适温度为30℃. 相似文献
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Tadakazu Takeo 《Bioscience, biotechnology, and biochemistry》2013,77(9):931-934
The effect of polyamide on the extraction of polyphenol oxidase in the leaves and the localization of the enzyme in tea leaf cell were investigated.In the homogenate treated with polyamide, a major part of the enzyme activity appeared in the centrifugal precipitates in the range of l,400×g to 15,000×g, and polyphenol content decreased. Therefore, it was thought that the enzyme in tea leaves existed primarily on the particle as small as mitochondria, but that it coagulated easily in the homogenate containing a high concentration of polyphenol, and precipitated by centrifugation at l,400×g.And also from the comparison of the ratio of the enzyme activity to chlorophyll concentration in each fraction separated by centrifugation, it was assumed that a major part of the enzyme did not exist in the chloroplast, but was bound on the precipitable particle in the range of l,400×g to 15,000×g. 相似文献
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Tadakazu Takeo 《Bioscience, biotechnology, and biochemistry》2013,77(12):1211-1214
A remarkable increase in polyphenol oxidase activity was observed in tea leaves after plucking. When the tea leaves treated with the specific inhibitors for the protein biosynthesis such as blasticidin S and puromycin A by the absorption through stem or by the vacuum infiltration, the increase in the enzyme activity was severely prevented. Therefore, it was thought that these antibiotics inhibited the activation of polyphenol oxidase. In addition, CM-cellulose column chromatogram of the enzyme protein of the withered leaves was different from that of the fresh leaves. It was also considered that new protein containing the enzyme activity developed in the withered leaves.These results suggest that the synthesis of the enzyme protein occurred in tea leaves after plucking. 相似文献
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Tadakazu Takeo 《Bioscience, biotechnology, and biochemistry》2013,77(6):558-563
The large part of the polyphenol oxidase was solubilized from tea leaf homogenate by addition of Tween-80. After filtration of the solubilized polyphenol oxidase fraction through a Sephadex G-25 column and fractionation of the filtrate with ammonium sulfate, the specific activity of the solubilized enzyme increased about 4 to 5 times as much as that of tea leaf homogenate. Optimum pH of the solubilized enzyme was 5.5, and was almost the same as that of water-insoluble enzyme in the acetone powder. The minimum concentrations required for the maximum activity were about 5×10?3 m, 4.3×10?3 m, and 3×10?3 m for d-catechin, l-epigallocatechin, and l-epigallocatechin-gallate, respectively. d-Catechin showed the highest activity among them. The enzyme activity was inhibited by potassium cyanide and sodium diethyldithiocarbamate. 相似文献
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普查了 7个科 11种植物的乙醇酸氧化酶 (GO) ,发现其酶蛋白与黄素单核苷酸 (FMN)的结合均是松弛的 ;并据此特征找到了一种温和的制备完全脱FMNGO的新方法 ,酶液总活性回收可达 87.5 % ;外加FMN可使脱辅因子GO不同程度地恢复活性 ,恢复 5 0 %活性所需FMN的浓度为 8× 10 -7mol/L ,而当浓度大于 5× 10 -6mol/L时其复活作用达到 10 0 % ,表明两者间存在一个可逆的解离平衡。推测植物体内的FMN浓度可能是乙醇酸氧化酶活性的一个调节因子。 相似文献
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The binding condition between flavin mononucleotide (FMN) and protein moiety of glycollate oxidase (GO) was investigated in 11 species of higher plants from 7 families. A loose binding of FMN with GO was universally observed in all the plants. According to this character, a new efficient but mild method was established for preparation of FMN-free GO, which could produce 87.5% recovery of activity . FMN-free GO could be reactivated by adding FMN. For half reactivation 8×10 mol/L FMN was needed, and more than 5×10 mol/L for 100%. The result indicates that there exists a reversible dissociation balance between FMN and protein moiety of GO. Therefore, the concentration of FMN may act as a factor to regulate GO activity in higher plants. 相似文献